Chain elongation in the isoprenoid biosynthetic pathway

被引:165
作者
Kellogg, BA [1 ]
Poulter, CD [1 ]
机构
[1] Univ Utah, Dept Chem, Salt Lake City, UT 84112 USA
关键词
D O I
10.1016/S1367-5931(97)80054-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Isoprenyl diphosphate synthases catalyze addition of allylic diphosphate primers to the isoprene unit in isopentenyl diphosphate to produce polyisoprenoid diphosphates with well defined chain lengths. Phylogenetic correlations suggest that the synthases which catalyze formation of isoprenoid diphosphates with (E) double bonds have evolved from a common ancestor. X-ray crystallographic studies of farnesyl diphosphate synthase in conjunction with site-directed mutagenesis have provided important new information about the residues involved in binding and catalysis and the source of chain length selectivity for the enzymes that catalyze chain elongation.
引用
收藏
页码:570 / 578
页数:9
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